简介：Transmissiblespongiformencephalopathyorpriondiseaseistriggeredbytheconversionfromcellularprionproteintopathogenicprionprotein.Growingevidencehasconcentratedonprionproteinconfigurationchangesandtheircorrelationwithpriondiseasetransmissibilityandpathogenicity.Invivoandinvitrostudieshaveshownthatseveralcytosolicformsofprionproteinwithspecifictopologicalstructurecandestroyintracellularstabilityandcontributetoprionproteinpathogenicity.Inthisstudy,thelatestmolecularchaperonesystemassociatedwithendoplasmicreticulum-associatedproteindegradation,theendoplasmicreticulumresidentproteinquality-controlsystemandtheubiquitinationproteasomesystem,isoutlined.Themolecularchaperonesystemdirectlycorrelateswiththeprionproteindegradationpathway.Understandingthemolecularmechanismswillhelpprovideafascinatingavenueforfurtherinvestigationsonpriondiseasetreatmentandprionprotein-inducedneurodegenerativediseases.